W S Allison - Concepedia

Author

W S Allison

University of California San Diego

Also Known As

W S Allison, W. S. Allison, W.S. Allison, Williams S. Allison

Publications

1.9K

Citations

H-Index

Concepts

All Affiliations

University of California San Diego Salk Institute for Biological Studies Brandeis University

About

W S Allison is an author at University of California San Diego specializing in biochemistry, natural sciences, and medicine.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Biochemistry	16	20	1.2K
2	Natural Sciences	15	18	1.1K
3	Medicine	14	15	899
4	Engineering	2	2	43
5	Health Sciences	1	1	48

W S Allison

Publications

1.8K

Citations

H-Index

Page 1

	Year	Citations
Identification of a tyrosine residue at a nucleotide binding site in the beta subunit of the mitochondrial ATPase with p-fluorosulfonyl[14C]-benzoyl-5'-adenosine. Frederick Esch, W S Allison Journal of Biological Chemistry Mitochondrial AtpaseLargest SubunitsBiochemistryMitochondrial FunctionTyrosine Residue	1978	207
The Mechanism of Inactivation of Glyceraldehyde 3-Phosphate Dehydrogenase by Tetrathionate, o-Iodosobenzoate, and Iodine Monochloride Douglas J. Parker, W S Allison Journal of Biological Chemistry Pig MuscleMetabolic PathwaysBioorganic ChemistryCellular EnzymologyBiochemistry	1969	137
Identification of an essential glutamic acid residue in the beta subunit of the adenosine triphosphatase from the thermophilic bacterium PS3. Minoru Yoshida, James W. Poser, W S Allison, Journal of Biological Chemistry Adenosine TriphosphataseIsolated SubunitsMolecular BiologySeveral PeptidesBiosynthesis	1981	118
The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide. Minoru Yoshida, W S Allison, Frederick Esch, Journal of Biological Chemistry Protein ChemistryMol.a Tryptic PeptideBiochemistryProtein FoldingNatural Sciences	1982	116
Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase. Jean‐Michel Jault, W S Allison Journal of Biological Chemistry	1993	113
Inactivation of the bovine heart mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyl[3H]inosine is accompanied by modification of tyrosine 345 in a single beta subunit. David A. Bullough, W S Allison Journal of Biological Chemistry	1986	104
Identification of the essential tyrosine residue in the beta subunit of bovine heart mitochondrial F1-ATPase that is modified by 7-chloro-4-nitro[14C]benzofurazan. William W. Andrews, Fred Hill, W S Allison Journal of Biological Chemistry Molecular BiologyMitochondrial BiologyRedox BiologyInactivated EnzymeEssential Tyrosine Residue	1984	99
Three copies of the beta subunit must be modified to achieve complete inactivation of the bovine mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyladenosine. David A. Bullough, W S Allison Journal of Biological Chemistry	1986	86
On the subunit stoichiometry of the F1-ATPase and the sites in it that react specifically with p-fluorosulfonylbenzoyl-5'-adenosine. Frederick Esch, W S Allison Journal of Biological Chemistry Beta SubunitsIncorporated LabelAldo-keto ReductaseCellular EnzymologyBiochemistry	1979	86
Identification of the lysine residue to which the 4-nitrobenzofurazan group migrates after the bovine mitochondrial F1-ATPase is inactivated with 7-chloro-4-nitro[14C]benzofurazan. William W. Andrews, Fred Hill, W S Allison Journal of Biological Chemistry	1984	84

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